The demand for enantiomerically pure pharmaceuticals, agrochemicals, and food additives is increasing due to the fact that different forms of enantiomers often have different behavior and can cause different biological effects.
Lipases are most useful in the preparation of enantiomerically pure compounds because lipase is comparatively economical and the lipase catalyzed process can be scaled up.
Although a large number of lipases have been evaluated for resolution of racemic alcohols and/or carboxylic acids, they have not generally met with great success due to low enantiospecificities. Various methodologies have been described to increase the enantioselectivity of lipase in resolution of racemates and immobilization of lipase is one of the methodologies.
U.S. Pat. No. 5,156,963 reports that immobilization of lipase on macroporous adsorbent resin of the acrylic type leads to a product with higher interesterification activity than prior art methods.
U.S. Pat. No. 5,445,955 reports that lipase or phospholipase immobilized on a macroporous adsorbent resin having an epoxy group on the surface thereof exhibits an excellent lipase activity, which is suitable for use for transesterification reaction in a system containing very small amount of water.
The above mentioned U.S. patents do not discuss about the enantioselectivity of the immobilized lipase.